5DB5
Crystal structure of PLP-bound E. coli SufS (cysteine persulfide intermediate) in space group P21
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001887 | biological_process | selenium compound metabolic process |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006534 | biological_process | cysteine metabolic process |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0008826 | molecular_function | cysteine sulfinate desulfinase activity |
| A | 0009000 | molecular_function | selenocysteine lyase activity |
| A | 0016226 | biological_process | iron-sulfur cluster assembly |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0031071 | molecular_function | cysteine desulfurase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0001887 | biological_process | selenium compound metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006534 | biological_process | cysteine metabolic process |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0008826 | molecular_function | cysteine sulfinate desulfinase activity |
| B | 0009000 | molecular_function | selenocysteine lyase activity |
| B | 0016226 | biological_process | iron-sulfur cluster assembly |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0031071 | molecular_function | cysteine desulfurase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue PLP A 501 |
| Chain | Residue |
| A | THR94 |
| A | HOH637 |
| B | GLY277 |
| B | THR278 |
| A | THR95 |
| A | HIS123 |
| A | ASN175 |
| A | ASP200 |
| A | ALA202 |
| A | GLN203 |
| A | SER223 |
| A | HIS225 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | ASP211 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue PLP B 501 |
| Chain | Residue |
| A | GLY277 |
| A | THR278 |
| B | THR94 |
| B | THR95 |
| B | HIS123 |
| B | ALA125 |
| B | ASN175 |
| B | ASP200 |
| B | ALA202 |
| B | GLN203 |
| B | SER223 |
| B | HIS225 |
| B | CIT503 |
| B | HOH657 |
| B | HOH666 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue CIT B 503 |
| Chain | Residue |
| A | HIS55 |
| A | THR278 |
| B | HIS123 |
| B | ASN175 |
| B | CSS364 |
| B | ARG379 |
| B | PLP501 |
| B | HOH612 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 20 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. CDFYvfSGHKlygpt.GiGiL |
| Chain | Residue | Details |
| A | CYS217-LEU236 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Cysteine persulfide intermediate |
| Chain | Residue | Details |
| A | CSS364 | |
| B | CSS364 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS226 | |
| B | LYS226 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 855 |
| Chain | Residue | Details |
| A | HIS123 | increase basicity, proton acceptor, proton donor |
| A | ASP200 | electrostatic stabiliser, polar interaction |
| A | GLN203 | electrostatic stabiliser, polar interaction |
| A | LYS226 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | CSS364 | covalently attached, nucleophile, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 855 |
| Chain | Residue | Details |
| B | HIS123 | increase basicity, proton acceptor, proton donor |
| B | ASP200 | electrostatic stabiliser, polar interaction |
| B | GLN203 | electrostatic stabiliser, polar interaction |
| B | LYS226 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | CSS364 | covalently attached, nucleophile, proton donor |
